期刊
SCIENCE
卷 336, 期 6079, 页码 320-323出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1218709
关键词
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资金
- EPFL
- Swiss National Science Foundation (FNS) [200020-130579]
- Science and Technology Swiss-Russian cooperation program
- Swiss National Science Foundation (SNF) [200020_130579] Funding Source: Swiss National Science Foundation (SNF)
Studying solvation of a large molecule on an atomic level is challenging because of the transient character and inhomogeneity of hydrogen bonding in liquid water. We studied water clusters of a protonated macrocyclic decapeptide, gramicidin S, which were prepared in the gas phase and then cooled to cryogenic temperatures. The experiment spectroscopically tracked fine structural changes of the clusters upon increasing the number of attached water molecules from 1 to 50 and distinguished vibrational fingerprints of different conformers. The data indicate that only the first two water molecules induce a substantial change of the gramicidin S structure by breaking two intramolecular noncovalent bonds. The peptide structure remains largely intact upon further solvation, reflecting the interplay between the strong intramolecular and weaker intermolecular hydrogen bonds.
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